Information on EC 2.4.1.128 - scopoletin glucosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.128
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RECOMMENDED NAME
GeneOntology No.
scopoletin glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + scopoletin = UDP + scopolin
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Phenylpropanoid biosynthesis
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superpathway of scopolin and esculin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:scopoletin O-beta-D-glucosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
81210-69-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
glycosyltransferases of family 1 are capable of transferring sugar moieties from activated sugar donors to a wide range of small lipophilic acceptors leading to an increase in water solubility, improved chemical stability and altered biological activity of the sugar conjugates, in plants, family 1 glycosyltransferases play an important role in metabolic homeostasis, regulation of phytohormone activities and detoxification of xenobiotics such as herbicides and pesticides; glycosyltransferases of family 1 are capable of transferring sugar moieties from activated sugar donors to a wide range of small lipophilic acceptors leading to an increase in water solubility, improved chemical stability and altered biological activity of the sugar conjugates, in plants, family l glycosyltransferases play an important role in metabolic homeostasis, regulation of phytohormone activities and detoxification of xenobiotics such as herbicides and pesticides
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
additional information
?
-
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the enzyme shows activity towards a number of coumarins including umbelliferone, scopoletin, isoscopoletin and esculetin, and flavonoids including a flavone, a flavanone and chalcones. No activity is detected with compounds characterized by a single aromatic ring, i.e. simple and acidic phenols
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + scopoletin
UDP + scopolin
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
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the addition of Na+ to buffered standard assays at concentration 1 and 10 mM has a stimulating effect on the glucosylation of scopoletin to 110% and 128%, respectively
additional information
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not affected by Mg2+ and Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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51.5% residual activity at 1 mM, 12% residual activity at 10 mM
Mn2+
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40.9% residual activity at 1 mM, complete inhibition at 10 mM
Zn2+
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27.1% residual activity at 1 mM, complete inhibition at 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dichlorophenoxyacetic acid
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0.005 mM, 10fold activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0152 - 0.112
scopoletin
0.2772 - 1.065
UDP-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 10.92
scopoletin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.21 - 210.7
scopoletin
1357
0.21 - 13.05
UDP-glucose
64
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00084
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activity in crude extracts
0.03
71C3, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30C
0.114
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cells cultured in the presence of 0.005 mM 2,4-dichlorophenoxyacetic acid
1.356
71C1, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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absent from isolated vacuoles, most probably located in the cytosol
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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native PAGE
51000
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x * 51000, SDS-PAGE
80000
by SDS-PAGE, approximate molecular weight of wild-type enzyme and mutants; by SDS-PAGE, approximate molecular weight of wild-type enzyme and mutants
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 51000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl-Sepharose column chromatographyand DEAE Sepharose column chromatography
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ammonium sulfate, Sephadex G-100, DEAE-cellulose, hydroxyapatite
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recombinant proteins are purified by affinity chromatography using GST-Sepharose 4B; recombinant proteins are purified by affinity chromatography using GST-Sepharose 4B
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, transgenic plants over-expressing the enzyme in leaves and in roots
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generation of plants overexpressing the enzyme. Over-expression leads to precocious lesion formation during the hypersensitive response to tobacco mosaic virus but does not affect virus resistance
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recombinant and mutant glycosyltransferase 71C1 is expressed as fusion protein tagged with a 26 kDa GST protein at the N-terminus in Escherichia coli BL21, production of a chimeric mutant derived from 2 Arabidopsis glucosyltransferases, 71C1 and 71C3, the chimera contains the N-terminal domain of 71C1 and the C-terminal domain of 71C3; recombinant and mutant glycosyltransferase 71C3 is expressed as fusion protein tagged with a 26 kDa GST protein at the N-terminus in Escherichia coli BL21, production of a chimeric mutant derived from 2 Arabidopsis glucosyltransferases, 71C1 and 71C3, the chimera contains the N-terminal domain of 71C1 and the C-terminal domain of 71C3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D257E/S260L
by site-directed mutagenesis
D262E/N265Q
by site-directed mutagenesis